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Rod cell | |
---|---|
Details | |
Location | Retina |
Shape | Rod-shaped |
Function | Low-light photoreceptor |
Neurotransmitter | Glutamate |
Presynaptic connections | None |
Postsynaptic connections | Bipolar cells and horizontal cells |
Identifiers | |
MeSH | D017948 |
NeuroLex ID | nlx_cell_100212 |
TH | H3.11.08.3.01030 |
FMA | 67747 |
Anatomical terms of neuroanatomy |
Rod cells are photoreceptor cells in the retina of the eye that can function in lower light better than the other type of visual photoreceptor, cone cells. Rods are usually found concentrated at the outer edges of the retina and are used in peripheral vision. On average, there are approximately 92 million rod cells (vs ~6 million cones) in the human retina. [1] Rod cells are more sensitive than cone cells and are almost entirely responsible for night vision. However, rods have little role in color vision, which is the main reason why colors are much less apparent in dim light.
Rods are a little longer and leaner than cones but have the same basic structure. Opsin-containing disks lie at the end of the cell adjacent to the retinal pigment epithelium, which in turn is attached to the inside of the eye. The stacked-disc structure of the detector portion of the cell allows for very high efficiency. Rods are much more common than cones, with about 120 million rod cells compared to 6 to 7 million cone cells. [2]
Like cones, rod cells have a synaptic terminal, an inner segment, and an outer segment. The synaptic terminal forms a synapse with another neuron, usually a bipolar cell or a horizontal cell. The inner and outer segments are connected by a cilium, [3] which lines the distal segment. [4] The inner segment contains organelles and the cell's nucleus, while the rod outer segment (abbreviated to ROS), which is pointed toward the back of the eye, contains the light-absorbing materials. [3]
A human rod cell is about 2 microns in diameter and 100 microns long. [5] Rods are not all morphologically the same; in mice, rods close to the outer plexiform synaptic layer display a reduced length due to a shortened synaptic terminal. [6]
In vertebrates, activation of a photoreceptor cell is a hyperpolarization (inhibition) of the cell. When they are not being stimulated, such as in the dark, rod cells and cone cells depolarize and release a neurotransmitter spontaneously. This neurotransmitter hyperpolarizes the bipolar cell. Bipolar cells exist between photoreceptors and ganglion cells and act to transmit signals from the photoreceptors to the ganglion cells. As a result of the bipolar cell being hyperpolarized, it does not release its transmitter at the bipolar-ganglion synapse and the synapse is not excited.
Activation of photopigments by light sends a signal by hyperpolarizing the rod cell, leading to the rod cell not sending its neurotransmitter, which leads to the bipolar cell then releasing its transmitter at the bipolar-ganglion synapse and exciting the synapse.
Depolarization of rod cells (causing release of their neurotransmitter) occurs because in the dark, cells have a relatively high concentration of cyclic guanosine 3'-5' monophosphate (cGMP), which opens ion channels (largely sodium channels, though calcium can enter through these channels as well). The positive charges of the ions that enter the cell down its electrochemical gradient change the cell's membrane potential, cause depolarization, and lead to the release of the neurotransmitter glutamate. Glutamate can depolarize some neurons and hyperpolarize others, allowing photoreceptors to interact in an antagonistic manner.
When light hits photoreceptive pigments within the photoreceptor cell, the pigment changes shape. The pigment, called rhodopsin (conopsin is found in cone cells) comprises a large protein called opsin (situated in the plasma membrane), attached to which is a covalently bound prosthetic group: an organic molecule called retinal (a derivative of vitamin A). The retinal exists in the 11-cis-retinal form when in the dark, and stimulation by light causes its structure to change to all-trans-retinal. This structural change causes an increased affinity for the regulatory protein called transducin (a type of G protein). Upon binding to rhodopsin, the alpha subunit of the G protein replaces a molecule of GDP with a molecule of GTP and becomes activated. This replacement causes the alpha subunit of the G protein to dissociate from the beta and gamma subunits of the G protein. As a result, the alpha subunit is now free to bind to the cGMP phosphodiesterase (an effector protein). [8] The alpha subunit interacts with the inhibitory PDE gamma subunits and prevents them from blocking catalytic sites on the alpha and beta subunits of PDE, leading to the activation of cGMP phosphodiesterase, which hydrolyzes cGMP (the second messenger), breaking it down into 5'-GMP. [9] Reduction in cGMP allows the ion channels to close, preventing the influx of positive ions, hyperpolarizing the cell, and stopping the release of the neurotransmitter glutamate. [3] Though cone cells primarily use the neurotransmitter substance acetylcholine, rod cells use a variety. The entire process by which light initiates a sensory response is called visual phototransduction.
Activation of a single unit of rhodopsin, the photosensitive pigment in rods, can lead to a large reaction in the cell because the signal is amplified. Once activated, rhodopsin can activate hundreds of transducin molecules, each of which in turn activates a phosphodiesterase molecule, which can break down over a thousand cGMP molecules per second. [3] Thus, rods can have a large response to a small amount of light.
As the retinal component of rhodopsin is derived from vitamin A, a deficiency of vitamin A causes a deficit in the pigment needed by rod cells. Consequently, fewer rod cells are able to sufficiently respond in darker conditions, and as the cone cells are poorly adapted for sight in the dark, night-blindness can result.
Rods make use of three inhibitory mechanisms (negative feedback mechanisms) to allow a rapid revert to the resting state after a flash of light.
Firstly, there exists a rhodopsin kinase (RK) which would phosphorylate the cytosolic tail of the activated rhodopsin on the multiple serines, partially inhibiting the activation of transducin. Also, an inhibitory protein, arrestin, then binds to the phosphorylated rhodopsins to further inhibit the rhodopsin activity.
While arrestin shuts off rhodopsin, an RGS protein (functioning as a GTPase-activating protein (GAP)) drives the transducin (G-protein) into an "off" state by increasing the rate of hydrolysis of the bonded GTP to GDP.
When the cGMP concentration falls, the previously open cGMP sensitive channels close, leading to a reduction in the influx of calcium ions. The associated decrease in the concentration of calcium ions stimulates the calcium ion-sensitive proteins, which then activate the guanylyl cyclase to replenish the cGMP, rapidly restoring it to its original concentration. This opens the cGMP sensitive channels and causes a depolarization of the plasma membrane. [10]
When the rods are exposed to a high concentration of photons for a prolonged period, they become desensitized (adapted) to the environment.
As rhodopsin is phosphorylated by rhodopsin kinase (a member of the GPCR kinases (GRKs) ), it binds with high affinity to the arrestin. The bound arrestin can contribute to the desensitization process in at least two ways. First, it prevents the interaction between the G protein and the activated receptor. Second, it serves as an adaptor protein to aid the receptor to the clathrin-dependent endocytosis machinery (to induce receptor-mediated endocytosis). [10]
A rod cell is sensitive enough to respond to a single photon of light [11] and is about 100 times more sensitive to a single photon than cones. Since rods require less light to function than cones, they are the primary source of visual information at night (scotopic vision). Cone cells, on the other hand, require tens to hundreds of photons to become activated. Additionally, multiple rod cells converge on a single interneuron, collecting and amplifying the signals. However, this convergence comes at a cost to visual acuity (or image resolution) because the pooled information from multiple cells is less distinct than it would be if the visual system received information from each rod cell individually.
Rod cells also respond more slowly to light than cones and the stimuli they receive are added over roughly 100 milliseconds. While this makes rods more sensitive to smaller amounts of light, it also means that their ability to sense temporal changes, such as quickly changing images, is less accurate than that of cones. [3]
Experiments by George Wald and others showed that rods are most sensitive to wavelengths of light around 498 nm (green-blue), and insensitive to wavelengths longer than about 640 nm (red). This is responsible for the Purkinje effect: as intensity dims at twilight, the rods take over, and before color disappears completely, peak sensitivity of vision shifts towards the rods' peak sensitivity (blue-green). [13]
The retina is the innermost, light-sensitive layer of tissue of the eye of most vertebrates and some molluscs. The optics of the eye create a focused two-dimensional image of the visual world on the retina, which then processes that image within the retina and sends nerve impulses along the optic nerve to the visual cortex to create visual perception. The retina serves a function which is in many ways analogous to that of the film or image sensor in a camera.
Rhodopsin, also known as visual purple, is a protein encoded by the RHO gene and a G-protein-coupled receptor (GPCR). It is the opsin of the rod cells in the retina and a light-sensitive receptor protein that triggers visual phototransduction in rods. Rhodopsin mediates dim light vision and thus is extremely sensitive to light. When rhodopsin is exposed to light, it immediately photobleaches. In humans, it is regenerated fully in about 30 minutes, after which the rods are more sensitive. Defects in the rhodopsin gene cause eye diseases such as retinitis pigmentosa and congenital stationary night blindness.
A photoreceptor cell is a specialized type of neuroepithelial cell found in the retina that is capable of visual phototransduction. The great biological importance of photoreceptors is that they convert light into signals that can stimulate biological processes. To be more specific, photoreceptor proteins in the cell absorb photons, triggering a change in the cell's membrane potential.
Transducin (Gt) is a protein naturally expressed in vertebrate retina rods and cones and it is very important in vertebrate phototransduction. It is a type of heterotrimeric G-protein with different α subunits in rod and cone photoreceptors.
In visual physiology, adaptation is the ability of the retina of the eye to adjust to various levels of light. Natural night vision, or scotopic vision, is the ability to see under low-light conditions. In humans, rod cells are exclusively responsible for night vision as cone cells are only able to function at higher illumination levels. Night vision is of lower quality than day vision because it is limited in resolution and colors cannot be discerned; only shades of gray are seen. In order for humans to transition from day to night vision they must undergo a dark adaptation period of up to two hours in which each eye adjusts from a high to a low luminescence "setting", increasing sensitivity hugely, by many orders of magnitude. This adaptation period is different between rod and cone cells and results from the regeneration of photopigments to increase retinal sensitivity. Light adaptation, in contrast, works very quickly, within seconds.
Guanylate cyclase is a lyase enzyme that converts guanosine triphosphate (GTP) to cyclic guanosine monophosphate (cGMP) and pyrophosphate:
As a part of the retina, bipolar cells exist between photoreceptors and ganglion cells. They act, directly or indirectly, to transmit signals from the photoreceptors to the ganglion cells.
Melanopsin is a type of photopigment belonging to a larger family of light-sensitive retinal proteins called opsins and encoded by the gene Opn4. In the mammalian retina, there are two additional categories of opsins, both involved in the formation of visual images: rhodopsin and photopsin in the rod and cone photoreceptor cells, respectively.
Cyclic nucleotide–gated ion channels or CNG channels are ion channels that function in response to the binding of cyclic nucleotides. CNG channels are nonselective cation channels that are found in the membranes of various tissue and cell types, and are significant in sensory transduction as well as cellular development. Their function can be the result of a combination of the binding of cyclic nucleotides and either a depolarization or a hyperpolarization event. Initially discovered in the cells that make up the retina of the eye, CNG channels have been found in many different cell types across both the animal and the plant kingdoms. CNG channels have a very complex structure with various subunits and domains that play a critical role in their function. CNG channels are significant in the function of various sensory pathways including vision and olfaction, as well as in other key cellular functions such as hormone release and chemotaxis. CNG channels have also been found to exist in prokaryotes, including many spirochaeta, though their precise role in bacterial physiology remains unknown.
Visual phototransduction is the sensory transduction process of the visual system by which light is detected by photoreceptor cells in the vertebrate retina. A photon is absorbed by a retinal chromophore, which initiates a signal cascade through several intermediate cells, then through the retinal ganglion cells (RGCs) comprising the optic nerve.
Horizontal cells are the laterally interconnecting neurons having cell bodies in the inner nuclear layer of the retina of vertebrate eyes. They help integrate and regulate the input from multiple photoreceptor cells. Among their functions, horizontal cells are believed to be responsible for increasing contrast via lateral inhibition and adapting both to bright and dim light conditions. Horizontal cells provide inhibitory feedback to rod and cone photoreceptors. They are thought to be important for the antagonistic center-surround property of the receptive fields of many types of retinal ganglion cells.
Intrinsically photosensitive retinal ganglion cells (ipRGCs), also called photosensitive retinal ganglion cells (pRGC), or melanopsin-containing retinal ganglion cells (mRGCs), are a type of neuron in the retina of the mammalian eye. The presence of an additional photoreceptor was first suspected in 1927 when mice lacking rods and cones still responded to changing light levels through pupil constriction; this suggested that rods and cones are not the only light-sensitive tissue. However, it was unclear whether this light sensitivity arose from an additional retinal photoreceptor or elsewhere in the body. Recent research has shown that these retinal ganglion cells, unlike other retinal ganglion cells, are intrinsically photosensitive due to the presence of melanopsin, a light-sensitive protein. Therefore, they constitute a third class of photoreceptors, in addition to rod and cone cells.
Congenital stationary night blindness (CSNB) is a rare non-progressive retinal disorder. People with CSNB often have difficulty adapting to low light situations due to impaired photoreceptor transmission. These patients may also have reduced visual acuity, myopia, nystagmus, fundus abnormalities, and strabismus. CSNB has two forms -- complete, also known as type-1 (CSNB1), and incomplete, also known as type-2 (CSNB2), which are distinguished by the involvement of different retinal pathways. In CSNB1, downstream neurons called bipolar cells are unable to detect neurotransmission from photoreceptor cells. CSNB1 can be caused by mutations in various genes involved in neurotransmitter detection, including NYX. In CSNB2, the photoreceptors themselves have impaired neurotransmission function; this is caused primarily by mutations in the gene CACNA1F, which encodes a voltage-gated calcium channel important for neurotransmitter release. CSNB has been identified in horses and dogs as the result of mutations in TRPM1, GRM6, and LRIT3 .
Rhodopsin kinase is a serine/threonine-specific protein kinase involved in phototransduction. This enzyme catalyses the following chemical reaction:
Retinylidene proteins, or rhodopsins in a broad sense, are proteins that use retinal as a chromophore for light reception. They are the molecular basis for a variety of light-sensing systems from phototaxis in flagellates to eyesight in animals. Retinylidene proteins include all forms of opsin and rhodopsin. While rhodopsin in the narrow sense refers to a dim-light visual pigment found in vertebrates, usually on rod cells, rhodopsin in the broad sense refers to any molecule consisting of an opsin and a retinal chromophore in the ground state. When activated by light, the chromophore is isomerized, at which point the molecule as a whole is no longer rhodopsin, but a related molecule such as metarhodopsin. However, it remains a retinylidene protein. The chromophore then separates from the opsin, at which point the bare opsin is a retinylidene protein. Thus, the molecule remains a retinylidene protein throughout the phototransduction cycle.
The visual cycle is a process in the retina that replenishes the molecule retinal for its use in vision. Retinal is the chromophore of most visual opsins, meaning it captures the photons to begin the phototransduction cascade. When the photon is absorbed, the 11-cis retinal photoisomerizes into all-trans retinal as it is ejected from the opsin protein. Each molecule of retinal must travel from the photoreceptor cell to the RPE and back in order to be refreshed and combined with another opsin. This closed enzymatic pathway of 11-cis retinal is sometimes called Wald's visual cycle after George Wald (1906–1997), who received the Nobel Prize in 1967 for his work towards its discovery.
Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta is the beta subunit of the protein complex PDE6 that is encoded by the PDE6B gene. PDE6 is crucial in transmission and amplification of visual signal. The existence of this beta subunit is essential for normal PDE6 functioning. Mutations in this subunit are responsible for retinal degeneration such as retinitis pigmentosa or congenital stationary night blindness.
S-arrestin is a protein that in humans is encoded by the SAG gene.
Mammals normally have a pair of eyes. Although mammalian vision is not so excellent as bird vision, it is at least dichromatic for most of mammalian species, with certain families possessing a trichromatic color perception.
Retinal degeneration is a retinopathy which consists in the deterioration of the retina caused by the progressive death of its cells. There are several reasons for retinal degeneration, including artery or vein occlusion, diabetic retinopathy, R.L.F./R.O.P., or disease. These may present in many different ways such as impaired vision, night blindness, retinal detachment, light sensitivity, tunnel vision, and loss of peripheral vision to total loss of vision. Of the retinal degenerative diseases retinitis pigmentosa (RP) is a very important example.